Identification of small peptides mimicking the R2 C-terminus of Mycobacterium tuberculosis ribonucleotide reductase

✍ Scribed by Daniel J. Ericsson; Johanna Nurbo; Daniel Muthas; Kalle Hertzberg; Gunnar Lindeberg; Anders Karlén; Torsten Unge

• Book ID: 105359844
• Publisher: John Wiley and Sons
• Year: 2010
• Tongue: English
• Weight: 386 KB
• Volume: 16
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.1214

✦ Synopsis

Abstract

Ribonucleotide reductase (RNR) is a viable target for new drugs against the causative agent of tuberculosis, Mycobacterium tuberculosis. Previous work has shown that an N‐acetylated heptapeptide based on the C‐terminal sequence of the smaller RNR subunit can disrupt the formation of the holoenzyme sufficiently to inhibit its function. Here the synthesis and binding affinity, evaluated by competitive fluorescence polarization, of several truncated and N‐protected peptides are described. The protected single‐amino acid Fmoc‐Trp shows binding affinity comparable to the N‐acetylated heptapeptide, making it an attractive candidate for further development of non‐peptidic RNR inhibitors. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.